In vitro assembly of mosaic hepatitis B virus capsid-like particles (CLPs): Rescue into CLPs of assembly-deficient core protein fusions and FRET-suited CLPs

摘要: Hepatitis B virus core protein self-assembles into icosahedral, highly immunogenic capsid-like particles (CLPs) that can serve as molecular platforms for heterologous proteins. Insertion the centrally located c/e1 epitope leads to surface display, fusion C terminus internal disposition of foreign domains. However, symmetry-defined space restrictions on and particularly inside CLPs limit size usable partners. Further, carrying differing domains are desirable applications such multivalent vaccines, structure probing by distance sensitive interactions like fluorescence resonance energy transfer (FRET). Here, we report an in vitro co-assembly system mosaic-CLPs allowing successful CLP formation with a per se assembly-deficient protein, from two different fluoroprotein-carrying fusions exert FRET assembly-status dependent way.